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PTX3 (human) Detection Set [for ELISA application], Enzo Life Sciences

Catalog Number: (89156-106)

Supplier: Enzo Life Sciences

Description: For the quantitative determination of PTX3 in human and bovine (weak) cell culture media, EDTA-plasma or serum (weak) samples.

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Mouse Recombinant CD40L (soluble)

Catalog Number: (89151-820)

Supplier: Enzo Life Sciences

Description: Produced in HEK 293 cells. The extracellular domain of mouse CD40L (CD154) (aa 115-260) is fused at the N-terminus to a linker peptide (8 aa) and a FLAG®-tag.

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Flagellin

Catalog Number: (89151-800)

Supplier: Enzo Life Sciences

Description: Isolated from Salmonella typhimurium strain 14028.

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Human Recombinant DcR3:Fc

Catalog Number: (89151-790)

Supplier: Enzo Life Sciences

Description: Produced in HEK 293 cells. The extracellular domain of human DcR3 (decoy receptor 3) (aa 1-246) is fused to the Fc portion of human IgG1.

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Human Recombinant Netrin 1

Catalog Number: (89151-870)

Supplier: Enzo Life Sciences

Description: Produced in HEK 293 cells. The extracellular domain of human netrin-1 (aa 28-604) is fused at the N-terminus to a FLAG®-tag.

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Human;Mouse Recombinant Thy-1 (RLE) (mouse):Fc

Catalog Number: (89151-860)

Supplier: Enzo Life Sciences

Description: Produced in HEK 293 cells. The extracellular domain of mouse Thy-1 (aa 20-131) is fused to the Fc portion of human IgG1. The integrin binding sequence RLD of mouse Thy-1 has been changed to RLE abolishing the binding of integrins.

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Lipopolysaccharides (from E.coli) serotype R515 (Re), TLRgrade™

Catalog Number: (89152-762)

Supplier: Enzo Life Sciences

Description: TLR4 activator.

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Anti-ESR2 Rabbit Polyclonal Antibody

Catalog Number: (89145-214)

Supplier: Enzo Life Sciences

Description: Host: Rabbit

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Anti-PSMB9 Mouse Monoclonal Antibody

Supplier: Enzo Life Sciences

Description: The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits. Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. Lmp2, Lmp7 and MECL are interferon gamma-inducible catalytic subunits of the 20S proteasome which may replace the constitutive catalytic subunits, delta, X and Z respectively, during proteasome biogenesis. Lmp2 and Lmp7 alter the cleavage site specificity of the 20S proteasome and are required for the efficient generation of T cell epitopes from a number of viral proteins and for optimal MHC class I cell surface expression.

Anti-Proteasome 19S Rpt1/S7 Subunit Mouse Monoclonal Antibody

Supplier: Enzo Life Sciences

Description: The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits. Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. In addition to the 20S particle, the 26S complex contains over twenty additional proteins, ranging in molecular weight from 25 to 10kDa, located in a distinct complex called the ‘PA700 proteasome activator’ or the ‘19S complex’, and which determines substrate specificity and provides the multiple enzymatic functions necessary for proteolysis and viability. Systematic analysis of the sub-unit components have revealed at least six members to be ATPases belonging to a new family of ATPbinding proteins, together with a further fifteen sub-units that lack the capacity to bind ATP, isopeptidases and several other proteins thought to be responsible for the unfolding of a protein substrate prior to insertion into the proteolytic core of the 20S proteasome.